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Cystine knot

A cystine knot is a protein structural motif containing three disulfide bridges. The sections of polypeptide that occur between two of them form a loop through which a third disulfide bond passes, forming a rotaxane-like substructure. The cystine knot motif stabilizes protein structure and is conserved in proteins across various species. There are three types of cystine knot, which differ in the topology of the disulfide bonds:Growth factor cystine knot (GFCK) Inhibitor cystine knot (ICK), common in spider and snail toxins Cyclic cystine knot, or cyclotide

Drug implications
The stability and structure of the cystine knot motif implicates possible applications in drug design. The disulfide bonds and the hydrogen bonding between the beta-sheet regions make the structure highly stable, and it has a fairly small size (around 30 amino acids). These two characteristics make it an attractive biomolecule to be used for drug delivery as it exhibits thermal stability, chemical stability, and proteolytic resistance. Studies have shown that cystine knot proteins can be incubated at temperatures of 65 °C or placed in 1N HCl/1N NaOH without loss of structural and functional integrity. Together with a partial resistance to proteases, these properties make cystine knot peptides attractive platforms for orally-dosed pharmaceuticals. == References ==
Source: Wikipedia ↗
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